TLPA_BRADU
ID TLPA_BRADU Reviewed; 221 AA.
AC P43221;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Thiol:disulfide interchange protein TlpA;
DE AltName: Full=Cytochrome c biogenesis protein TlpA;
GN Name=tlpA; OrderedLocusNames=bll1380;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=8253065; DOI=10.1002/j.1460-2075.1993.tb06011.x;
RA Loferer H., Bott M., Hennecke H.;
RT "Bradyrhizobium japonicum TlpA, a novel membrane-anchored thioredoxin-like
RT protein involved in the biogenesis of cytochrome aa3 and development of
RT symbiosis.";
RL EMBO J. 12:3373-3383(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
RN [3]
RP CHARACTERIZATION, AND DISULFIDE BOND.
RX PubMed=8055901; DOI=10.1111/j.1432-1033.1994.tb18999.x;
RA Loferer H., Hennecke H.;
RT "Expression, purification and functional properties of a soluble form of
RT Bradyrhizobium japonicum TlpA, a thioredoxin-like protein.";
RL Eur. J. Biochem. 223:339-344(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 36-221, AND DISULFIDE BONDS.
RX PubMed=11531338; DOI=10.1006/jmbi.2001.4913;
RA Capitani G., Rossmann R., Sargent D.F., Gruetter M.G., Richmond T.J.,
RA Hennecke H.;
RT "Structure of the soluble domain of a membrane-anchored thioredoxin-like
RT protein from Bradyrhizobium japonicum reveals unusual properties.";
RL J. Mol. Biol. 311:1037-1048(2001).
CC -!- FUNCTION: Involved in cytochrome aa3 assembly.
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC P43221; Q89VB6: blr1131; NbExp=3; IntAct=EBI-8146602, EBI-8146640;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
CC protein; Periplasmic side.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z23140; CAA80671.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC46645.1; -; Genomic_DNA.
DR PIR; S40401; S40401.
DR RefSeq; NP_768020.1; NC_004463.1.
DR RefSeq; WP_011084198.1; NZ_CP011360.1.
DR PDB; 1JFU; X-ray; 1.60 A; A/B=36-221.
DR PDB; 4TXO; X-ray; 2.20 A; A/C/E/G=38-221.
DR PDB; 4TXV; X-ray; 2.00 A; A/C=40-217.
DR PDBsum; 1JFU; -.
DR PDBsum; 4TXO; -.
DR PDBsum; 4TXV; -.
DR AlphaFoldDB; P43221; -.
DR SMR; P43221; -.
DR IntAct; P43221; 1.
DR MINT; P43221; -.
DR STRING; 224911.27349631; -.
DR EnsemblBacteria; BAC46645; BAC46645; BAC46645.
DR GeneID; 64021250; -.
DR KEGG; bja:bll1380; -.
DR PATRIC; fig|224911.44.peg.803; -.
DR eggNOG; COG0526; Bacteria.
DR HOGENOM; CLU_042529_11_0_5; -.
DR InParanoid; P43221; -.
DR OMA; VPCRKEM; -.
DR PhylomeDB; P43221; -.
DR EvolutionaryTrace; P43221; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytochrome c-type biogenesis; Disulfide bond;
KW Membrane; Redox-active center; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..221
FT /note="Thiol:disulfide interchange protein TlpA"
FT /id="PRO_0000120177"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..221
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 69..215
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 45..190
FT DISULFID 107..110
FT /note="Redox-active"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1JFU"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:1JFU"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1JFU"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:1JFU"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1JFU"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:1JFU"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:1JFU"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:1JFU"
FT HELIX 108..124
FT /evidence="ECO:0007829|PDB:1JFU"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:1JFU"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:1JFU"
FT HELIX 165..171
FT /evidence="ECO:0007829|PDB:1JFU"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:1JFU"
FT STRAND 177..185
FT /evidence="ECO:0007829|PDB:1JFU"
FT STRAND 189..197
FT /evidence="ECO:0007829|PDB:1JFU"
FT HELIX 204..214
FT /evidence="ECO:0007829|PDB:1JFU"
SQ SEQUENCE 221 AA; 23260 MW; DD4C7EADF2F0FE1B CRC64;
MLDTKPSATR RIPLVIATVA VGGLAGFAAL YGLGLSRAPT GDPACRAAVA TAQKIAPLAH
GEVAALTMAS APLKLPDLAF EDADGKPKKL SDFRGKTLLV NLWATWCVPC RKEMPALDEL
QGKLSGPNFE VVAINIDTRD PEKPKTFLKE ANLTRLGYFN DQKAKVFQDL KAIGRALGMP
TSVLVDPQGC EIATIAGPAE WASEDALKLI RAATGKAAAA L
